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Effect of Amino Acid Substitutions at a Site of Temperature Sensitive Folding Mutation of P22 Tailspike Protein

Molecules and Cells 1990년 1권 1호 p.93 ~ 98
 ( Park Joo-Sang ) - Korea Institute of Science and Technology Genetic Engineering Center

 ( Koh Hye-Yeong ) - Korea Institute of Science and Technology Genetic Engineering Center
 ( Yu Myeong-Hee ) - Korea Institute of Science and Technology Genetic Engineering Center

Abstract


Twelve different single amino acid substitutions were made at the site of a temperature sensitive folding mutation, TsfU2 (Asp238→Ser), of the phage P22 tailspike protein. Most of the substitutions except Pro and Arg did not affect folding and maturation of the tailspike protein at 28 ℃. However, at 39 ℃ only the wild type residue, Asp, and the Thr substitution allowed the formation of the tailspike trimers. The results suggest that a stereospecific interaction of the residue 238 is required for the folding and maturation of the tailspike, which is critical for stabilizing the folding intermediate at high temperature.

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